(data stored in SCRATCH zone)

SWISSPROT: Q82RP2_STRAW

ID   Q82RP2_STRAW            Unreviewed;      1244 AA.
AC   Q82RP2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAY-2019, entry version 110.
DE   SubName: Full=Putative polyketide synthase (Type-II AT + aminotransferase) {ECO:0000313|EMBL:BAC67810.1};
GN   Name=pks11-2 {ECO:0000313|EMBL:BAC67810.1};
GN   ORFNames=SAVERM_101 {ECO:0000313|EMBL:BAC67810.1};
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS   NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC67810.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC67810.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2] {ECO:0000313|EMBL:BAC67810.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00612749};
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DR   EMBL; BA000030; BAC67810.1; -; Genomic_DNA.
DR   RefSeq; WP_010981537.1; NC_003155.5.
DR   STRING; 227882.SAV_101; -.
DR   EnsemblBacteria; BAC67810; BAC67810; SAVERM_101.
DR   KEGG; sma:SAVERM_101; -.
DR   eggNOG; ENOG4107EEK; Bacteria.
DR   eggNOG; COG0156; LUCA.
DR   OrthoDB; 572620at2; -.
DR   BioCyc; SAVE227882:G1G23-115-MONOMER; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
DR   PRODOM; Q82RP2.
DR   SWISS-2DPAGE; Q82RP2.
KW   Aminotransferase {ECO:0000313|EMBL:BAC67810.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000428};
KW   Phosphopantetheine {ECO:0000256|PROSITE-ProRule:PRU00258};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00473492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW   Transferase {ECO:0000313|EMBL:BAC67810.1}.
FT   DOMAIN      659    737       Carrier. {ECO:0000259|PROSITE:PS50075}.
FT   MOD_RES     697    697       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   1244 AA;  130118 MW;  26DFCC9FC36316E9 CRC64;
     MLISAGSPRL LDGQIGELLD FLDRSPGTPP AAMAHTLGGR EMLTARLAVV AATPDELAGR
     LRRARRQLAD GVRGDLGDGA FAADAPLPPE QRRIAFVFPG QGSQRPAMMH DLYQRSGLFR
     AALDTLGAPA REHTGLSPAQ VLYGQRASTP PGDAQLRQRP AGTDVCQPLL GSVQIAATRL
     LAACGVSPDL TLGHSAGEFA AAAAAGALTD EDTVRLLAHR GAALAQAETG ARGGMLAVQS
     DKETCRRLVH GIDDVWFACF NHPRQVVVSG TVQGLAALRR ACAAAKVAAV TLEVSNAFHS
     PRLASAEAAM RADLARRPVT RPPVAFVSCV SAALCSDPAE LRELWARHAC APVRFEEAVR
     SAYAHGARVF LQVTGNRSLL ASVRRSLAGH GDVRLAGTDG PAPDSGRGFL QALAHLAVLG
     APVDPRALIP QQDRRLLDLP VARLDTQSYW IRQPRRPATP VNPVNPVNPV NPVNNEAPTA
     GVPLRPAPFG PCGAPRTEQP ATGRTTAGET TGEATGETTG QTAGEADGQA DGPATWQATG
     QEVLHEALTL LREQGALLTR LSEALGTHHA TGPAAQSEAL PIASTAPAAS APPAPAASGI
     PAVPAVRCAP PADDDPAAAS ADADRPAARN ITDITQIREA AEATKVSEAT EATEAGEAAE
     AAEAAETVFA HVARISAFPI SHLHGRQLLT DDLGFDSLML TDLFASLKRQ WPFLTIDEKT
     YDRPTVEGLI TMITDGSADT APLTAPRTRP TGRREAADAL AAPQAVTEPN AEPNAGPGAG
     PGAGPDAGPD GDALPDPPAV GPHAVPPTRT GLHAVPPAHT GLHAVPAART GPATAGLPEQ
     QTQIECFPEV TAHNERLATY SRLGLPNPYF VVHERGMTDT TVVGGRELLS FSSYNYLGMA
     THPQVNEAAR KAIERCGTSV SASRLLSGSR PLHLELEAEL AATLGCEAAI TLVNGHATNV
     TVIGHLVGEG DLIVHDSLAH DSIIQGCRLS GARRRPFPHN DAAALDALLT QVRHHYRRVL
     VVAEGVYSMD GDIADLPALI EVKRRHGALL MIDEAHSIGV IGAAGRGIGQ YFDVDRQDVE
     LWSGTLSKAL ASCGGYVAAG RTVVDYLRYT VPGFVFSAGM TPANTAASLA ALRVLRAEPQ
     RVARLKENSA LFARLAHRAG IDTGPSHDTP IIPCIVGDSA KTLQLAEALF EQGISVNPIL
     YPAVPEKAAR LRFFITCDHT PDQIHHTVRE LAHGLRQADT APAA
//

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